Protein Structure And Proteins : Proteins

Different types of bonds/interactions in proteins lead to different kinds of structures. Three of the most commonly known chemical bonds in proteins include the hydrogen bond, the covalent bond, and the ionic bond. In hydrogen bonds, hydrogen interacts with oxygen, nitrogen, or fluorine to form either the alpha helix, or the beta sheet, which in turn determines its secondary, tertiary, or quaternary structure. Another type of bonds, the covalent bond, links amino acids together by sharing electrons;

Proteins are polymers made by joining up small molecules called amino acids. Amino acids and proteins are made mainly of the elements carbon, hydrogen, oxygen and nitrogen.

Proteins are the metabolic workhorses of the cell; they engage in a variety of essential activities ranging from enzymatically catabolizing macromolecular food sources to serving as structural components that maintain cell stability. Maximizing protein function relies on intricate non-covalent interactions occurring on the secondary, tertiary, and quaternary levels that help determine the overall shape of the protein. In their native states, proteins will assume the most energetically favorable configuration. Occasionally however, cells are exposed to exogenous disruptions such as heat stress. Heat Stress can compromise protein three-dimensional structure. Hydrophobic residues tend to be buried in the interior of the protein but when

3. Explain why the structure of a protein is important to how the protein functions. It’s important because it can make many complex shape and each shapes can have different functions.

The chaperones have the main role of ensuring proper folding. When a chaperone protein becomes toxic, major changes in the conformation occur as the alpha helix becomes beta pleated sheets. The sheets now expose the hydrophobic amino acid and aggregation, or clumping together of sheets occurs (Borges, 2014).

Proteins are complex structures made up of chains of amino acids. Each protein has a different function such as enzymes to catalyze reactions or protein hormones to trigger certain functions of a cell. First let’s start with the most basic component of a protein: an amino acid. An amino acid is made up of a central carbon atom attached to a hydrogen atom, a carboxyl group, an amino group, and an R group which varies

their normal shape to an abnormal shape, however, the chemical composition of the protein remains

They are made up of amino acids (consists of amino group, carboxyl group, hydrogen atom, and R group). Polypeptide bonds form between amino acids to form polypeptide chains. Amino acid sequence is primary protein structure. The secondary structure is the bonding pattern of the amino acids (e.g. helix, sheet, etc.). The tertiary structure consists of the domain, where the sheets or helixes fold on each other and become stable. The quaternary structure consists of several polypeptide chains that form advanced proteins such as human leukocyte

Proteins are polymeric chains that are built from monomers called amino acids. All structural and functional properties of proteins derive from the chemical properties of the polypeptide chain. There are four levels of protein structural organization: primary, secondary, tertiary, and quaternary. Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results from long-range contacts within the chain. The quaternary structure is the organization of protein subunits, or two or more independent polypeptide chains.

. The 3-D tertiary structure of polypeptide proteins globular and is the result of interactions that occur between R groups. Tertiary structure is a result of the bonds between sidechains of amino acids, the R groups. The structure and bonds involve alpha helices, beta pleated sheets, and also regions unique to each protein. Tertiary proteins are held together by four different types of forces; hydrogen bonds, hydrophobic interactions (including Van der Waals interactions), ionic bonding (electrostatic interactions), and disulfide bridges (strong covalent bonds). Hydrogen bonds occur within and between polypeptide chains and the aqueous environment. Hydrogen bonding forms between a highly electronegative oxygen atom or a nitrogen atom and a hydrogen atom attached to another oxygen atom or a nitrogen atom. This links the amino acid

This folding describes the arrangement of the amino acids. The shape of the acids is held in place by the hydrogen bonds. A hydrogen bond is a dipole-dipole interaction between a hydrogen atom and an electronegative atom. The hydrogen bonds are important because if they didn’t hold the structure of the amino acids in place, there would be no backbone for the protein.

Enzyme are protein that folded from many linear chain of amino acid. The sequence of the amino acids specifies the structure which

The primary structure of a protein is the sequence of amino acids. This creates a polypeptide chain because each amino acid acts as a monomer so when they bind together they form a polymer. When amino acids bond together, a peptide bond is formed. This occurs when there is a condensation reaction and H2O is lost from the two amino acids and a bond forms between the carbon on one amino acid and the

Campbell and Farrell define proteins as polymers of amino acids that have been covalently joined through peptide bonds to form amino acid chains (61). A short amino acid chain comprising of thirty amino acids forms a peptide, and a longer chain of amino acids forms a polypeptide or a protein. Each of the amino acids making up a protein, has a fundamental design that comprises of a central carbon or alpha carbon that is bonded to a hydrogen element, an amino grouping, a carboxyl grouping, and a unique side chain or the R-group (Campbell and Farrell 61).

Protein synthesis is one of the most fundamental biological processes. To start off, a protein is made in a ribosome. There are many cellular mechanisms involved with protein synthesis. Before the process of protein synthesis can be described, a person must know what proteins are made out of. There are four basic levels of protein organization. The first is primary structure, followed by secondary structure, then tertiary structure, and the last level is quaternary structure. Once someone understands the makeup of a protein, they can then begin to learn how elements can combine and go from genes to protein. There are two main processes that occur during protein synthesis, or peptide formation. One is transcription and